3PXU

Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei bound to dephospho-coenzyme A

Replaces:  3IKZ

Summary for 3PXU

• Entry DOI: 10.2210/pdb3pxu/pdb
• Related: 3K9W
• Descriptor: Phosphopantetheine adenylyltransferase, DEPHOSPHO COENZYME A, GLYCEROL, ... (5 entities in total)
• Functional Keywords: structural genomics, seattle structural genomics center for infectious disease, ssgcid, human and animal pathogen, melioidosis, atp-binding, coenzyme a biosynthesis, nucleotide-binding, nucleotidyltransferase, transferase, ppat, pantetheine-phosphate adenylyltransferase
• Biological source: Burkholderia pseudomallei
• Cellular location: Cytoplasm : Q3JW91
• Total number of polymer chains: 1
• Total formula weight: 19913.52

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-12-10, release date: 2010-12-22, Last modification date: 2023-09-13)

Primary citation

Edwards, T.E.,Leibly, D.J.,Bhandari, J.,Statnekov, J.B.,Phan, I.,Dieterich, S.H.,Abendroth, J.,Staker, B.L.,Van Voorhis, W.C.,Myler, P.J.,Stewart, L.J.
Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei.
Acta Crystallogr.,Sect.F, 67:1032-1037, 2011

PubMed Abstract: Phosphopantetheine adenylyltransferase (PPAT) catalyzes the fourth of five steps in the coenzyme A biosynthetic pathway, reversibly transferring an adenylyl group from ATP onto 4'-phosphopantetheine to yield dephospho-coenzyme A and pyrophosphate. Burkholderia pseudomallei is a soil- and water-borne pathogenic bacterium and the etiologic agent of melioidosis, a potentially fatal systemic disease present in southeast Asia. Two crystal structures are presented of the PPAT from B. pseudomallei with the expectation that, because of the importance of the enzyme in coenzyme A biosynthesis, they will aid in the search for defenses against this pathogen. A crystal grown in ammonium sulfate yielded a 2.1 Å resolution structure that contained dephospho-coenzyme A with partial occupancy. The overall structure and ligand-binding interactions are quite similar to other bacterial PPAT crystal structures. A crystal grown at low pH in the presence of coenzyme A yielded a 1.6 Å resolution structure in the same crystal form. However, the experimental electron density was not reflective of fully ordered coenzyme A, but rather was only reflective of an ordered 4'-diphosphopantetheine moiety.

PubMed: 21904046
DOI: 10.1107/S1744309111004349

Experimental method

X-RAY DIFFRACTION (2.1 Å)